Major facilitator superfamily domain-containing protein 8
Major facilitator superfamily (MFS) domain-containing protein 8 (MFSD8) is also called ceroid-lipofuscinosis neuronal protein 7 (CLN7). It is a polytopic lysosomal membrane protein that may transport small solutes by using chemiosmotic ion gradients. Mutations in MFSD8/CLN7 cause a variant of late-infantile neuronal ceroid lipofuscinoses (vLINCL), a neurodegenerative lysosomal storage disorder. Some variants are associated with nonsyndromic autosomal recessive macular dystrophy. MFSD8/CLN7 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance -like (SLC46/TetA-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Feature 1:putative chemical substrate binding pocket [chemical binding site]
Evidence:
Comment:based on the structures of MFS transporters with bound substrates, substrate analogs, and/or inhibitors
Comment:since MFS proteins facilitate the transport of many different substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides, the residues involved in substrate binding may not be strictly conserved among superfamily members
Comment:the substrate binding site or translocation pore has access to both sides of the membrane in an alternating fashion through a conformational change of the MFS transporter
Jiyao W et al.(2023). "The conserved domain database in 2023.",